Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

Nikolaus Falb; Dominik Hörtnagel; Chris Oostenbrink; Paul G. Furtmüller; Stefan Hofbauer

doi:10.1111/febs.70575

May 6, 2026FEBS JournalOpen Access

Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

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Key Points

This research aims to investigate the role of the loop in the wild-type conformation of coproheme decarboxylase in substrate transfer regulation.
Analyzing the structural conformation of coproheme decarboxylase from Listeria monocytogenes
Examining the interaction between active site and cosubstrates
The loop in wild-type conformation significantly regulates cosubstrate transfer toward coproheme.
Evidence of the loop's critical role suggests implications for enzymatic function and substrate specificity.

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Implication

Study reveals active site regulation of coproheme transfer in Listeria monocytogenes, indicating functional significance.

Abstract

, suggesting the loop in its wild-type conformation plays a key biological role in regulating the transfer of cosubstrates towards the main substrate coproheme.

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Cite This Study

Falb et al. (2026) studied this question.

synapsesocial.com/papers/69fd7f86bfa21ec5bbf08017 https://doi.org/10.1111/febs.70575

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Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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